3IKO

Crystal structure of the heterotrimeric Sec13-Nup145C-Nup84 nucleoporin complex

Summary for 3IKO

• Entry DOI: 10.2210/pdb3iko/pdb
• Descriptor: Protein transport protein SEC13, Nucleoporin NUP145C, Nucleoporin NUP84 (3 entities in total)
• Functional Keywords: npc, transport, wd repeat, autocatalytic cleavage, mrna transport, nuclear pore complex, nucleus, phosphoprotein, translocation, protein transport, coiled coil, membrane, hydrolase, rna-binding, cytoplasmic vesicle, endoplasmic reticulum, er-golgi transport, nuclear protein, structural protein
• Biological source: Saccharomyces cerevisiae (yeast); More
• Cellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side: Q04491; Nucleoporin NUP145C: Nucleus, nuclear pore complex. Nucleoporin NUP145N: Nucleus, nuclear pore complex: P49687; Nucleus, nuclear pore complex: P52891
• Total number of polymer chains: 9
• Total formula weight: 410884.97

Authors

Nagy, V.,Hsia, K.-C.,Debler, E.W.,Davenport, A.,Blobel, G.,Hoelz, A. (deposition date: 2009-08-06, release date: 2009-10-13, Last modification date: 2024-02-21)

Primary citation

Nagy, V.,Hsia, K.C.,Debler, E.W.,Kampmann, M.,Davenport, A.M.,Blobel, G.,Hoelz, A.
Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.
Proc.Natl.Acad.Sci.USA, 106:17693-17698, 2009

PubMed Abstract: The heptameric Nup84 complex constitutes an evolutionarily conserved building block of the nuclear pore complex. Here, we present the crystal structure of the heterotrimeric Sec13 x Nup145C x Nup84 complex, the centerpiece of the heptamer, at 3.2-A resolution. Nup84 forms a U-shaped alpha-helical solenoid domain, topologically similar to two other members of the heptamer, Nup145C and Nup85. The interaction between Nup84 and Nup145C is mediated via a hydrophobic interface located in the kink regions of the two solenoids that is reinforced by additional interactions of two long Nup84 loops. The Nup84 binding site partially overlaps with the homo-dimerization interface of Nup145C, suggesting competing binding events. Fitting of the elongated Z-shaped heterotrimer into electron microscopy (EM) envelopes of the heptamer indicates that structural changes occur at the Nup145C x Nup84 interface. Docking the crystal structures of all heptamer components into the EM envelope constitutes a major advance toward the completion of the structural characterization of the Nup84 complex.

PubMed: 19805193
DOI: 10.1073/pnas.0909373106

Experimental method

X-RAY DIFFRACTION (3.2 Å)